4an5: Difference between revisions

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'''Unreleased structure'''


The entry 4an5 is ON HOLD
==Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly==
<SX load='4an5' size='340' side='right' viewer='molstar' caption='[[4an5]], [[Resolution|resolution]] 8.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4an5]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_SPP1 Bacillus phage SPP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AN5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 8.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4an5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4an5 OCA], [https://pdbe.org/4an5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4an5 RCSB], [https://www.ebi.ac.uk/pdbsum/4an5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4an5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CAPSD_BPSPP CAPSD_BPSPP] Capsid protein self-assembles, with the help of the scaffolding protein gp11, to form an icosahedral capsid with a T=7 symmetry, about 61 nm in diameter. The capsid encapsulates the genomic DNA.<ref>PMID:10656821</ref> <ref>PMID:22514336</ref>
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== Publication Abstract from PubMed ==
The structure of the bacteriophage SPP1 capsid was determined at subnanometer resolution by cryo-electron microscopy and single-particle analysis. The icosahedral capsid is composed of the major capsid protein gp13 and the auxiliary protein gp12, which are organized in a T=7 lattice. DNA is arranged in layers with a distance of ~24.5 A. gp12 forms spikes that are anchored at the center of gp13 hexamers. In a gp12-deficient mutant, the centers of hexamers are closed by loops of gp13 coming together to protect the SPP1 genome from the outside environment. The HK97-like fold was used to build a pseudoatomic model of gp13. Its structural organization remains unchanged upon tail binding and following DNA release. gp13 exhibits enhanced thermostability in the DNA-filled capsid. A remarkable convergence between the thermostability of the capsid and those of the other virion components was found, revealing that the overall architecture of the SPP1 infectious particle coevolved toward high robustness.


Authors: White, H.E., Sherman, M.B., Brasiles, S., Jacquet, E., Seavers, P., Tavares, P., Orlova, E.V.
Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly.,White HE, Sherman MB, Brasiles S, Jacquet E, Seavers P, Tavares P, Orlova EV J Virol. 2012 Jun;86(12):6768-77. Epub 2012 Apr 18. PMID:22514336<ref>PMID:22514336</ref>


Description: Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4an5" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Bacillus phage SPP1]]
[[Category: Large Structures]]
[[Category: Brasiles S]]
[[Category: Jacquet E]]
[[Category: Orlova EV]]
[[Category: Seavers P]]
[[Category: Sherman MB]]
[[Category: Tavares P]]
[[Category: White HE]]

Latest revision as of 13:52, 9 May 2024

Capsid structure and its Stability at the Late Stages of Bacteriophage SPP1 AssemblyCapsid structure and its Stability at the Late Stages of Bacteriophage SPP1 Assembly

4an5, resolution 8.80Å

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